References
- Finder VH, Glockshuber R. Amyloid-beta aggregation. Neurodegener Dis 2007;4:13–27
- Willander H, Presto J, Askarieh G, Biverstål H, Frohm B, Knight SD, Johansson J, et al. BRICHOS domains efficiently delay fibrillation of amyloid β-peptide. J Biol Chem 2012;287:31608–17
- Cohen SI, Arosio P, Presto J, Kurudenkandy FR, Biverstål H, Dolfe L, Dunning C, et al. A molecular chaperone breaks the catalytic cycle that generates toxic Aβoligomers. Nat Struct Mol Biol 2015;22:207–13
- Arosio P, Michaels TC, Linse S, Månsson C, Emanuelsson C, Presto J, Johansson J, et al. Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation. Nat Commun 2016;7:10948
- Poska H, Haslbeck M, Kurudenkandy FR, Hermansson E, Chen G, Kostallas G, Abelein A, et al. Dementia related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila. Biochem J 2016;473:3683–704
- Hermansson E, Schultz S, Crowther D, Linse S, Winblad B, Westermark G, Johansson J, et al. The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster. Dis Model Mech 2014;7:659–65